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Protein

Epididymal-specific lipocalin-9

Gene

Lcn9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Epididymal-specific lipocalin-9
Alternative name(s):
MUP-like lipocalin
Gene namesi
Name:Lcn9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1924954. Lcn9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 178162Epididymal-specific lipocalin-9PRO_0000017919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence analysis
Glycosylationi68 – 681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi83 ↔ 176By similarity
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9D267.
PRIDEiQ9D267.

Expressioni

Tissue specificityi

Expressed in epididymis. Not detected in all other tissues tested.1 Publication

Developmental stagei

First detected after 3 weeks postnatal development.1 Publication

Gene expression databases

BgeeiQ9D267.
CleanExiMM_LCN9.
GenevisibleiQ9D267. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023978.

Structurei

3D structure databases

ProteinModelPortaliQ9D267.
SMRiQ9D267. Positions 24-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JBWS. Eukaryota.
ENOG4111AS1. LUCA.
GeneTreeiENSGT00530000063356.
HOGENOMiHOG000231458.
HOVERGENiHBG000215.
InParanoidiQ9D267.
OMAiWYSIFMA.
OrthoDBiEOG77WWF8.
PhylomeDBiQ9D267.
TreeFamiTF338197.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002971. Maj_urinary.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01221. MAJORURINARY.
SUPFAMiSSF50814. SSF50814. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D267-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLLVLGLV LSLATAQFNL HTAVRRDYNL ARISGTWYLD SIASDNMTRI
60 70 80 90 100
EENGDLRLFI RNIKLLNNGS LQFDFHFMLQ GECVAVTMVC EKTKNNGEFS
110 120 130 140 150
VAYEGKNKVL LLETDYSMYI IFYMQNIKNG TKTQVLALYG RSILLDKTHQ
160 170
REFENICNLY GLDSQNIIDM TKKDFCFL
Length:178
Mass (Da):20,503
Last modified:June 1, 2001 - v1
Checksum:i400AD2D4658A93FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681N → I in AAO50215 (PubMed:15363845).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF435738 mRNA. Translation: AAO50215.1.
AK020305 mRNA. Translation: BAB32064.1.
CCDSiCCDS15792.1.
RefSeqiNP_084235.1. NM_029959.2.
UniGeneiMm.159974.

Genome annotation databases

EnsembliENSMUST00000023978; ENSMUSP00000023978; ENSMUSG00000023210.
GeneIDi77704.
KEGGimmu:77704.
UCSCiuc008itm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF435738 mRNA. Translation: AAO50215.1.
AK020305 mRNA. Translation: BAB32064.1.
CCDSiCCDS15792.1.
RefSeqiNP_084235.1. NM_029959.2.
UniGeneiMm.159974.

3D structure databases

ProteinModelPortaliQ9D267.
SMRiQ9D267. Positions 24-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023978.

Proteomic databases

PaxDbiQ9D267.
PRIDEiQ9D267.

Protocols and materials databases

DNASUi77704.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023978; ENSMUSP00000023978; ENSMUSG00000023210.
GeneIDi77704.
KEGGimmu:77704.
UCSCiuc008itm.1. mouse.

Organism-specific databases

CTDi392399.
MGIiMGI:1924954. Lcn9.

Phylogenomic databases

eggNOGiENOG410JBWS. Eukaryota.
ENOG4111AS1. LUCA.
GeneTreeiENSGT00530000063356.
HOGENOMiHOG000231458.
HOVERGENiHBG000215.
InParanoidiQ9D267.
OMAiWYSIFMA.
OrthoDBiEOG77WWF8.
PhylomeDBiQ9D267.
TreeFamiTF338197.

Miscellaneous databases

PROiQ9D267.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D267.
CleanExiMM_LCN9.
GenevisibleiQ9D267. MM.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002971. Maj_urinary.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01221. MAJORURINARY.
SUPFAMiSSF50814. SSF50814. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular evolution of epididymal lipocalin genes localized on mouse chromosome 2."
    Suzuki K., Lareyre J.-J., Sanchez D., Gutierrez G., Araki Y., Matusik R.J., Orgebin-Crist M.-C.
    Gene 339:49-59(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6 X DBA/2.
    Tissue: Epididymis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Epididymis.

Entry informationi

Entry nameiLCN9_MOUSE
AccessioniPrimary (citable) accession number: Q9D267
Secondary accession number(s): Q80ZC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.